1WYY

Post-fusion hairpin conformation of the sars coronavirus spike glycoprotein

Summary for 1WYY

• Entry DOI: 10.2210/pdb1wyy/pdb
• Descriptor: E2 Glycoprotein, CHLORIDE ION (3 entities in total)
• Functional Keywords: membrane fusion, severe acute respiratory syndrome, viral protein
• Biological source: SARS coronavirus; More
• Cellular location: Virion membrane ; Single-pass type I membrane protein : P59594
• Total number of polymer chains: 2
• Total formula weight: 32467.69

Authors

Duquerroy, S.,Vigouroux, A.,Rottier, P.J.M.,Rey, F.A.,Bosch, B.J. (deposition date: 2005-02-18, release date: 2005-05-17, Last modification date: 2023-10-25)

Primary citation

Duquerroy, S.,Vigouroux, A.,Rottier, P.J.M.,Rey, F.A.,Bosch, B.J.
Central ions and lateral asparagine/glutamine zippers stabilize the post-fusion hairpin conformation of the SARS coronavirus spike glycoprotein
Virology, 335:276-285, 2005

PubMed Abstract: The coronavirus spike glycoprotein is a class I membrane fusion protein with two characteristic heptad repeat regions (HR1 and HR2) in its ectodomain. Here, we report the X-ray structure of a previously characterized HR1/HR2 complex of the severe acute respiratory syndrome coronavirus spike protein. As expected, the HR1 and HR2 segments are organized in antiparallel orientations within a rod-like molecule. The HR1 helices form an exceptionally long (120 A) internal coiled coil stabilized by hydrophobic and polar interactions. A striking arrangement of conserved asparagine and glutamine residues of HR1 propagates from two central chloride ions, providing hydrogen-bonding "zippers" that strongly constrain the path of the HR2 main chain, forcing it to adopt an extended conformation at either end of a short HR2 alpha-helix.

PubMed: 15840526
DOI: 10.1016/j.virol.2005.02.022

Experimental method

X-RAY DIFFRACTION (2.2 Å)